VAPA_BOVIN
ID VAPA_BOVIN Reviewed; 249 AA.
AC Q0VCY1;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Vesicle-associated membrane protein-associated protein A;
DE Short=VAMP-A;
DE Short=VAMP-associated protein A;
DE Short=VAP-A;
GN Name=VAPA {ECO:0000250|UniProtKB:Q9P0L0};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAI19938.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford {ECO:0000312|EMBL:AAI19938.1};
RC TISSUE=Fetal muscle {ECO:0000312|EMBL:AAI19938.1};
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Binds to OSBPL3, which mediates recruitment of VAPA to plasma
CC membrane sites. The ORP3-VAPA complex stimulates RRAS signaling which
CC in turn attenuates integrin beta-1 (ITGB1) activation at the cell
CC surface. With OSBPL3, may regulate ER morphology. May play a role in
CC vesicle trafficking. {ECO:0000250|UniProtKB:Q9P0L0}.
CC -!- SUBUNIT: Homodimer, and heterodimer with VAPB. Interacts with VAMP1,
CC VAMP2, STX1A, BET1, SEC22C and with the C-terminal domain of OCLN.
CC Interacts with OSBPL1A. Interacts (via MSP domain) with ZFYVE27; may
CC retain ZFYVE27 in the endoplasmic reticulum and regulate its function
CC in cell projections formation. Interacts with OSBP. Interacts (via C-
CC terminus) with RSAD2/viperin (via C-terminus). Interacts with OSBPL3
CC (phosphorylated form). Interacts with STARD3 (via FFAT motif).
CC Interacts with STARD3NL (via FFAT motif). Interacts with CERT1 (By
CC similarity). Interacts with PLEKHA3 and SACM1L to form a ternary
CC complex (By similarity). Interacts with VPS13A (via FFAT motif) (By
CC similarity). {ECO:0000250|UniProtKB:Q9P0L0,
CC ECO:0000250|UniProtKB:Q9Z270}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9P0L0}; Single-pass type IV membrane protein
CC {ECO:0000250|UniProtKB:Q9P0L0}. Cell junction, tight junction
CC {ECO:0000250|UniProtKB:Q9P0L0}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9P0L0}; Single-pass type IV membrane protein
CC {ECO:0000305}. Note=Present in the plasma membrane and in intracellular
CC vesicles, together with SNARE proteins. May also associate with the
CC cytoskeleton. Colocalizes with OCLN at the tight junction in polarized
CC epithelial cells. {ECO:0000250|UniProtKB:Q9P0L0}.
CC -!- SIMILARITY: Belongs to the VAMP-associated protein (VAP) (TC 9.B.17)
CC family. {ECO:0000305}.
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DR EMBL; BC119937; AAI19938.1; -; mRNA.
DR RefSeq; NP_001069201.1; NM_001075733.1.
DR AlphaFoldDB; Q0VCY1; -.
DR SMR; Q0VCY1; -.
DR STRING; 9913.ENSBTAP00000022970; -.
DR PaxDb; Q0VCY1; -.
DR PeptideAtlas; Q0VCY1; -.
DR PRIDE; Q0VCY1; -.
DR Ensembl; ENSBTAT00000022970; ENSBTAP00000022970; ENSBTAG00000017279.
DR GeneID; 516024; -.
DR KEGG; bta:516024; -.
DR CTD; 9218; -.
DR VEuPathDB; HostDB:ENSBTAG00000017279; -.
DR VGNC; VGNC:36763; VAPA.
DR eggNOG; KOG0439; Eukaryota.
DR GeneTree; ENSGT00940000154799; -.
DR HOGENOM; CLU_032848_0_1_1; -.
DR InParanoid; Q0VCY1; -.
DR OMA; QSVIAPE; -.
DR OrthoDB; 1332028at2759; -.
DR TreeFam; TF317024; -.
DR Proteomes; UP000009136; Chromosome 24.
DR Bgee; ENSBTAG00000017279; Expressed in longissimus thoracis muscle and 105 other tissues.
DR ExpressionAtlas; Q0VCY1; baseline.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0033149; F:FFAT motif binding; IBA:GO_Central.
DR GO; GO:0008219; P:cell death; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0070972; P:protein localization to endoplasmic reticulum; ISS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR000535; MSP_dom.
DR InterPro; IPR008962; PapD-like_sf.
DR InterPro; IPR016763; VAP.
DR PANTHER; PTHR10809; PTHR10809; 2.
DR Pfam; PF00635; Motile_Sperm; 1.
DR PIRSF; PIRSF019693; VAMP-associated; 1.
DR SUPFAM; SSF49354; SSF49354; 1.
DR PROSITE; PS50202; MSP; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cell junction; Cell membrane; Coiled coil;
KW Endoplasmic reticulum; Membrane; Phosphoprotein; Reference proteome;
KW Tight junction; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9P0L0"
FT CHAIN 2..249
FT /note="Vesicle-associated membrane protein-associated
FT protein A"
FT /id="PRO_0000271378"
FT TOPO_DOM 2..227
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT DOMAIN 14..131
FT /note="MSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00132"
FT COILED 169..205
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0L0"
FT MOD_RES 125
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0L0"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0L0"
FT MOD_RES 170
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0L0"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0L0"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0L0"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0L0"
SQ SEQUENCE 249 AA; 27856 MW; E8E9081C1A5B85CB CRC64;
MASASGTMAK HEQILVLDPP TDLKFKGPFT DVVTTNLKLR NPSDRKVCFK VKTTAPRRYC
VRPNSGIIDP GLTVTVSVML QPFDYDPNEK SKHKFMVQTI FAPPNISDME AVWKEAKPDE
LMDSKLRCVF EMPNENDKLN DMEPSKAVPL NAAKQDGPVP KPHSVSLSDT ETRKLVEECK
RLQGEMMKLS EENRLLRDEG LRLRKVAHSE KPGSTSAVSF RENVTSPLPS LLVVIAAIFI
GFFLGKFIL
